The Influence of Lipid on the Conformation of Human Plasma High Density Apolipoproteins

The interaction of human plasma high density apolipoproteins (apoHDL) with lipids was examined by circular dichroism (CD) of the peptide and aromatic chromophores. By CD criteria native HDL contained about 70% α helical, 5 to 15% β, and 15 to 20% disordered structure. Delipidation decreased the helical content by about 20% with a corresponding increase in disordered structure. The two major apoproteins of HDL (apoA-I and apoA-II), isolated by chromatography in urea, refolded to different extents after removal of urea; apoA-I had more ordered structure than apoA-II (approximately 55% and 35% α helix, respectively). Reconstitution of apoA-I, apoA-II, and apoHDL with both phosphatidylcholine and cholesteryl ester restored, respectively, 119%, 87%, and 100% of the helical structure of the parent HDL. Phosphatidylcholine alone restored 50 to 70% of the increase produced by both phosphatidylcholine and cholesteryl oleate. With each substrate, the increase in helical content on lipid-protein recombination was accompanied by a corresponding decrease in disordered structure.